HEADER HYDROLASE 15-APR-07 2PJA
TITLE CRYSTAL STRUCTURE OF ACTIVATED PORCINE PANCREATIC CARBOXYPEPTIDASE B
TITLE 2 3-{[(R)-1-((S)-2-BENZYLOXYCARBONYLAMINO-3-PHENYL-PROPIONYLAMINO)-2-
TITLE 3 METHYL-PROPYL]-HYDROXY-PHOSPHINOYL}-2-(3-GUANIDINO-PHENYL)-PROPIONIC
TITLE 4 ACID COMPLEX
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CARBOXYPEPTIDASE B;
COMPND 3 CHAIN: A, B, C;
COMPND 4 FRAGMENT: CATALYTIC DOMAIN;
COMPND 5 EC: 3.4.17.2
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SUS SCROFA;
SOURCE 3 ORGANISM_COMMON: PIG;
SOURCE 4 ORGANISM_TAXID: 9823
KEYWDS CARBOXYPEPTIDASE B, EXOPEPTIDASE, PHOSPHINATE BASED INHIBITOR,
KEYWDS 2 HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR M.ADLER,M.WHITLOW
REVDAT 4 30-AUG-23 2PJA 1 REMARK
REVDAT 3 24-FEB-09 2PJA 1 VERSN
REVDAT 2 10-JUN-08 2PJA 1 JRNL
REVDAT 1 22-JAN-08 2PJA 0
JRNL AUTH M.ADLER,B.BUCKMAN,J.BRYANT,Z.CHANG,K.CHU,K.EMAYAN,P.HRVATIN,
JRNL AUTH 2 I.ISLAM,J.MORSER,D.SUKOVICH,C.WEST,S.YUAN,M.WHITLOW
JRNL TITL STRUCTURES OF POTENT SELECTIVE PEPTIDE MIMETICS BOUND TO
JRNL TITL 2 CARBOXYPEPTIDASE B.
JRNL REF ACTA CRYSTALLOGR.,SECT.D V. 64 149 2008
JRNL REFN ISSN 0907-4449
JRNL PMID 18219114
JRNL DOI 10.1107/S0907444907057228
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH M.ADLER,J.BRYANT,B.BUCKMAN,I.ISLAM,B.LARSEN,S.FINSTER,
REMARK 1 AUTH 2 L.KENT,K.MAY,R.MOHAN,S.YUAN,M.WHITLOW
REMARK 1 TITL CRYSTAL STRUCTURES OF POTENT THIOL-BASED INHIBITORS BOUND TO
REMARK 1 TITL 2 CARBOXYPEPTIDASE B.
REMARK 1 REF BIOCHEMISTRY V. 44 9339 2005
REMARK 1 REFN ISSN 0006-2960
REMARK 1 REFERENCE 2
REMARK 1 AUTH I.ISLAM,J.BRYANT,K.MAY,R.MOHAN,S.YUAN,L.KENT,J.MORSER,
REMARK 1 AUTH 2 L.ZHAO,R.VERGONA,K.WHITE,M.ADLER,M.WHITLOW,B.O.BUCKMAN
REMARK 1 TITL 3-MERCAPTOPROPIONIC ACIDS AS EFFICACIOUS INHIBITORS OF
REMARK 1 TITL 2 ACTIVATED THROMBIN ACTIVATABLE FIBRINOLYSIS INHIBITOR
REMARK 1 TITL 3 (TAFIA).
REMARK 1 REF BIOORG.MED.CHEM.LETT. V. 17 1349 2007
REMARK 1 REFN ISSN 0960-894X
REMARK 2
REMARK 2 RESOLUTION. 1.70 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNX 2005
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,
REMARK 3 : READ,RICE,SIMONSON,WARREN,ACCELRYS
REMARK 3 : SOFTWARE INC.(BADGER,BERARD,KUMAR,SZALMA,
REMARK 3 : YIP,DZAKULA)
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.70
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 21.40
REMARK 3 DATA CUTOFF (SIGMA(F)) : 2.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 2421454.560
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 94.8
REMARK 3 NUMBER OF REFLECTIONS : 92221
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING + TEST SET) : 0.190
REMARK 3 R VALUE (WORKING SET) : 0.189
REMARK 3 FREE R VALUE : 0.219
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.000
REMARK 3 FREE R VALUE TEST SET COUNT : 3653
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.004
REMARK 3
REMARK 3 FIT/AGREEMENT OF MODEL WITH ALL DATA.
REMARK 3 R VALUE (WORKING + TEST SET, NO CUTOFF) : 0.2270
REMARK 3 R VALUE (WORKING SET, NO CUTOFF) : 0.2260
REMARK 3 FREE R VALUE (NO CUTOFF) : 0.249
REMARK 3 FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : 4.000
REMARK 3 FREE R VALUE TEST SET COUNT (NO CUTOFF) : 3689
REMARK 3 ESTIMATED ERROR OF FREE R VALUE (NO CUTOFF) : 0.0040
REMARK 3 TOTAL NUMBER OF REFLECTIONS (NO CUTOFF) : 93160
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 10
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.70
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.76
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 87.30
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 8040
REMARK 3 BIN R VALUE (WORKING SET) : 0.2490
REMARK 3 BIN FREE R VALUE : 0.2730
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 3.80
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 316
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.015
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 7308
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 135
REMARK 3 SOLVENT ATOMS : 624
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 17.60
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 21.30
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.92000
REMARK 3 B22 (A**2) : 6.78000
REMARK 3 B33 (A**2) : -7.70000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.18
REMARK 3 ESD FROM SIGMAA (A) : 0.17
REMARK 3 LOW RESOLUTION CUTOFF (A) : 5.00
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.22
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.19
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.010
REMARK 3 BOND ANGLES (DEGREES) : 0.800
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 21.10
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.670
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : RESTRAINED
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : 1.090 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 1.520 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 1.860 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 2.710 ; 2.500
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.36
REMARK 3 BSOL : 45.40
REMARK 3
REMARK 3 NCS MODEL : NULL
REMARK 3
REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL
REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL
REMARK 3
REMARK 3 PARAMETER FILE 1 : PROTEIN_REP.P
REMARK 3 PARAMETER FILE 2 : WATER_REP.PAR
REMARK 3 PARAMETER FILE 3 : ZN.PAR
REMARK 3 PARAMETER FILE 4 : 333.PAR
REMARK 3 PARAMETER FILE 5 : NULL
REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 2 : WATER.TOP
REMARK 3 TOPOLOGY FILE 3 : ZN.TOP
REMARK 3 TOPOLOGY FILE 4 : 333.TOP
REMARK 3 TOPOLOGY FILE 5 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2PJA COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 25-APR-07.
REMARK 100 THE DEPOSITION ID IS D_1000042437.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 24-APR-01
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 6.50
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SSRL
REMARK 200 BEAMLINE : BL7-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.080
REMARK 200 MONOCHROMATOR : SI(111)
REMARK 200 OPTICS : SI(111)
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : MAR SCANNER 345 MM PLATE
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 93217
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.700
REMARK 200 RESOLUTION RANGE LOW (A) : 21.400
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 96.2
REMARK 200 DATA REDUNDANCY : 3.500
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.08700
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 7.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.70
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.74
REMARK 200 COMPLETENESS FOR SHELL (%) : 89.1
REMARK 200 DATA REDUNDANCY IN SHELL : 3.40
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.35300
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.200
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: FOURIER SYNTHESIS
REMARK 200 SOFTWARE USED: X-PLOR
REMARK 200 STARTING MODEL: PDB ENTRY 1Z5R
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 41.41
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.10
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: SODIUM CHLORIDE, TRIS, SODIUM
REMARK 280 CACODYLATE, PEG 8000, PH 6.50, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 X+1/2,-Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 33.48200
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 67.82050
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 48.18950
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 67.82050
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 33.48200
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 48.18950
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 3
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 THR A 4
REMARK 465 THR A 5
REMARK 465 THR B 4
REMARK 465 THR B 5
REMARK 465 THR C 4
REMARK 465 THR C 5
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 ASN A 58 64.24 34.26
REMARK 500 LYS A 122 -51.27 -137.00
REMARK 500 SER A 199 -18.08 155.38
REMARK 500 ASN A 215 34.94 -97.54
REMARK 500 ILE A 247 -62.27 -130.26
REMARK 500 ASP A 273 -139.62 -110.65
REMARK 500 ILE A 280 54.37 -94.39
REMARK 500 LYS B 122 -47.32 -131.85
REMARK 500 SER B 199 -13.56 151.69
REMARK 500 GLN B 200 70.21 54.93
REMARK 500 ASN B 215 35.43 -97.79
REMARK 500 ILE B 247 -72.87 -126.15
REMARK 500 ALA B 250 114.72 -166.11
REMARK 500 ASP B 273 -140.64 -106.45
REMARK 500 ILE B 280 54.17 -94.95
REMARK 500 LYS C 122 -62.13 -132.74
REMARK 500 THR C 129 -175.31 -68.92
REMARK 500 SER C 199 -15.48 151.74
REMARK 500 ASN C 215 36.14 -99.71
REMARK 500 ILE C 247 -74.94 -118.04
REMARK 500 ASP C 273 -142.26 -109.51
REMARK 500 ILE C 280 58.28 -91.76
REMARK 500 HIS C 307 48.03 -142.99
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 400
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 500
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN C 600
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 33Z A 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 33Z B 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 33Z C 601
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1Z5R RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF ACTIVATED PORCINE PANCREATIC CARBOXYPEPTIDASE B
REMARK 900 RELATED ID: 1ZG7 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF 2-(5-{[AMINO(IMINO)METHYL]AMINO}-2-
REMARK 900 CHLOROPHENYL)-3-SULFANYLPROPANOIC ACID BOUND TO ACTIVATED PORCINE
REMARK 900 PANCREATIC CARBOXYPEPTIDASE B
REMARK 900 RELATED ID: 1ZG8 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF (R)-2-(3-{[AMINO(IMINO)METHYL]AMINO}PHENYL)-3-
REMARK 900 SULFANYLPROPANOIC ACID BOUND TO ACTIVATED PORCINE PANCREATIC
REMARK 900 CARBOXYPEPTIDASE B
REMARK 900 RELATED ID: 1ZG9 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF 5-{[AMINO(IMINO)METHYL]AMINO}-2-
REMARK 900 (SULFANYLMETHYL)PENTANOIC ACID BOUND TO ACTIVATED PORCINE
REMARK 900 PANCREATIC CARBOXYPEPTIDASE B
REMARK 900 RELATED ID: 2PIY RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF ACTIVATED PORCINE PANCREATIC CARBOXYPEPTIDASE
REMARK 900 B (S)-2-(3-AMINOMETHYL-PHENYL)-3-{HYDROXY-[(R)-2-METHYL-1-(3-PHENYL-
REMARK 900 PROPANE-1-SULFONYLAMINO)-PROPYL]-PHOSPHINOYL}-PROPIONIC ACID {ZK
REMARK 900 528} COMPLEX
REMARK 900 RELATED ID: 2PIZ RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF ACTIVATED PORCINE PANCREATIC CARBOXYPEPTIDASE
REMARK 900 B 2-(3-GUANIDINO-PHENYL)-3-[HYDROXY-(3-PHENYL-PROPYL)-PHOSPHINOYL]-
REMARK 900 PROPIONIC ACID COMPLEX
REMARK 900 RELATED ID: 2PJ0 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF ACTIVATED PORCINE PANCREATIC CARBOXYPEPTIDASE
REMARK 900 B [((R)-1-BENZYLOXYCARBONYLAMINO-2-METHYL-PROPYL)-HYDROXY-
REMARK 900 PHOSPHINOYLOXY]-(3-GUANIDINO-PHENYL)-ACETIC ACID COMPLEX
REMARK 900 RELATED ID: 2PJ1 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF ACTIVATED PORCINE PANCREATIC CARBOXYPEPTIDASE
REMARK 900 B (3-AMINOMETHYL-PHENYL)-[((R)-1-BENZYLOXYCARBONYLAMINO-2-METHYL-
REMARK 900 PROPYL)-HYDROXY-PHOSPHINOYLOXY]-ACETIC ACID COMPLEX
REMARK 900 RELATED ID: 2PJ2 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF ACTIVATED PORCINE PANCREATIC CARBOXYPEPTIDASE
REMARK 900 B 2-(3-AMINOMETHYL-PHENYL)-3-[((R)-1-BENZYLOXYCARBONYLAMINO-2-
REMARK 900 METHYL-PROPYL)-HYDROXY-PHOSPHINOYL]-PROPIONIC ACID COMPLEX
REMARK 900 RELATED ID: 2PJ3 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF ACTIVATED PORCINE PANCREATIC CARBOXYPEPTIDASE
REMARK 900 B (3-GUANIDINO-PHENYL)-{HYDROXY-[(R)-2-METHYL-1-(3-PHENYL-
REMARK 900 PROPIONYLAMINO)-PROPYL]-PHOSPHINOYLOXY}-ACETIC ACID COMPLEX
REMARK 900 RELATED ID: 2PJ4 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF ACTIVATED PORCINE PANCREATIC CARBOXYPEPTIDASE
REMARK 900 B [((R)-BENZYLOXYCARBONYLAMINO-CYCLOHEXYL-METHYL)-HYDROXY-
REMARK 900 PHOSPHINOYLOXY]-(3-GUANIDINO-PHENYL)-ACETIC ACID COMPLEX
REMARK 900 RELATED ID: 2PJ5 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF ACTIVATED PORCINE PANCREATIC CARBOXYPEPTIDASE
REMARK 900 B [((R)-1-BENZYLOXYCARBONYLAMINO-HEXYL)-HYDROXY-PHOSPHINOYLOXY]-(3-
REMARK 900 GUANIDINO-PHENYL)-ACETIC ACID COMPLEX
REMARK 900 RELATED ID: 2PJ6 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF ACTIVATED PORCINE PANCREATIC CARBOXYPEPTIDASE
REMARK 900 B 2-(3-AMINOMETHYL-PHENYL)-3-{HYDROXY-[(R)-2-METHYL-1-(2-PHENYL-
REMARK 900 ETHANESULFONYLAMINO)-PROPYL]-PHOSPHINOYL}-PROPIONIC ACID COMPLEX
REMARK 900 RELATED ID: 2PJ7 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF ACTIVATED PORCINE PANCREATIC CARBOXYPEPTIDASE
REMARK 900 B 2-(3-AMINOMETHYL-PHENYL)-3-[((R)-1-BENZENESULFONYLAMINO-2-METHYL-
REMARK 900 PROPYL)-HYDROXY-PHOSPHINOYL]-PROPIONIC ACID COMPLEX
REMARK 900 RELATED ID: 2PJ8 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF ACTIVATED PORCINE PANCREATIC CARBOXYPEPTIDASE
REMARK 900 B 2-(3-AMINOMETHYL-PHENYL)-3-{[(R)-1-(BIPHENYL-4-SULFONYLAMINO)-2-
REMARK 900 METHYL-PROPYL]-HYDROXY-PHOSPHINOYL}-PROPIONIC ACID COMPLEX
REMARK 900 RELATED ID: 2PJ9 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF ACTIVATED PORCINE PANCREATIC CARBOXYPEPTIDASE
REMARK 900 B 2-(3-AMINOMETHYL-PHENYL)-3-{[(R)-1-(BENZO[1,2,5]THIADIAZOLE-4-
REMARK 900 SULFONYLAMINO)-2-METHYL-PROPYL]-HYDROXY-PHOSPHINOYL}-PROPIONIC ACID
REMARK 900 COMPLEX
REMARK 900 RELATED ID: 2PJB RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF ACTIVATED PORCINE PANCREATIC CARBOXYPEPTIDASE
REMARK 900 B 2-(3-AMINOMETHYL-PHENYL)-3-{[1-((S)-2-BENZYLOXYCARBONYLAMINO-3-
REMARK 900 PHENYL-PROPANE-1-SULFONYLAMINO)-2-METHYL-PROPYL]-HYDROXY-
REMARK 900 PHOSPHINOYL}-PROPIONIC ACID COMPLEX
REMARK 900 RELATED ID: 2PJC RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF ACTIVATED PORCINE PANCREATIC CARBOXYPEPTIDASE
REMARK 900 B ({(R)-1-[(S)-2-BENZYLOXYCARBONYLAMINO-3-(4-HYDROXY-PHENYL)-
REMARK 900 PROPIONYLAMINO]-2-METHYL-PROPYL}-HYDROXY-PHOSPHINOYLOXY)-(3-
REMARK 900 GUANIDINO-PHENYL)-ACETIC ACID COMPLEX
DBREF 2PJA A 4 308 UNP P09955 CBPB1_PIG 111 416
DBREF 2PJA B 4 308 UNP P09955 CBPB1_PIG 111 416
DBREF 2PJA C 4 308 UNP P09955 CBPB1_PIG 111 416
SEQRES 1 A 306 THR THR GLY HIS SER TYR GLU LYS TYR ASN ASN TRP GLU
SEQRES 2 A 306 THR ILE GLU ALA TRP THR LYS GLN VAL THR SER GLU ASN
SEQRES 3 A 306 PRO ASP LEU ILE SER ARG THR ALA ILE GLY THR THR PHE
SEQRES 4 A 306 LEU GLY ASN ASN ILE TYR LEU LEU LYS VAL GLY LYS PRO
SEQRES 5 A 306 GLY PRO ASN LYS PRO ALA ILE PHE MET ASP CYS GLY PHE
SEQRES 6 A 306 HIS ALA ARG GLU TRP ILE SER HIS ALA PHE CYS GLN TRP
SEQRES 7 A 306 PHE VAL ARG GLU ALA VAL LEU THR TYR GLY TYR GLU SER
SEQRES 8 A 306 HIS MET THR GLU PHE LEU ASN LYS LEU ASP PHE TYR VAL
SEQRES 9 A 306 LEU PRO VAL LEU ASN ILE ASP GLY TYR ILE TYR THR TRP
SEQRES 10 A 306 THR LYS ASN ARG MET TRP ARG LYS THR ARG SER THR ASN
SEQRES 11 A 306 ALA GLY THR THR CYS ILE GLY THR ASP PRO ASN ARG ASN
SEQRES 12 A 306 PHE ASP ALA GLY TRP CYS THR THR GLY ALA SER THR ASP
SEQRES 13 A 306 PRO CYS ASP GLU THR TYR CYS GLY SER ALA ALA GLU SER
SEQRES 14 A 306 GLU LYS GLU THR LYS ALA LEU ALA ASP PHE ILE ARG ASN
SEQRES 15 A 306 ASN LEU SER SER ILE LYS ALA TYR LEU THR ILE HIS SER
SEQRES 16 A 306 TYR SER GLN MET ILE LEU TYR PRO TYR SER TYR ASP TYR
SEQRES 17 A 306 LYS LEU PRO GLU ASN ASN ALA GLU LEU ASN ASN LEU ALA
SEQRES 18 A 306 LYS ALA ALA VAL LYS GLU LEU ALA THR LEU TYR GLY THR
SEQRES 19 A 306 LYS TYR THR TYR GLY PRO GLY ALA THR THR ILE TYR PRO
SEQRES 20 A 306 ALA ALA GLY GLY SER ASP ASP TRP ALA TYR ASP GLN GLY
SEQRES 21 A 306 ILE LYS TYR SER PHE THR PHE GLU LEU ARG ASP LYS GLY
SEQRES 22 A 306 ARG TYR GLY PHE ILE LEU PRO GLU SER GLN ILE GLN ALA
SEQRES 23 A 306 THR CYS GLU GLU THR MET LEU ALA ILE LYS TYR VAL THR
SEQRES 24 A 306 ASN TYR VAL LEU GLY HIS LEU
SEQRES 1 B 306 THR THR GLY HIS SER TYR GLU LYS TYR ASN ASN TRP GLU
SEQRES 2 B 306 THR ILE GLU ALA TRP THR LYS GLN VAL THR SER GLU ASN
SEQRES 3 B 306 PRO ASP LEU ILE SER ARG THR ALA ILE GLY THR THR PHE
SEQRES 4 B 306 LEU GLY ASN ASN ILE TYR LEU LEU LYS VAL GLY LYS PRO
SEQRES 5 B 306 GLY PRO ASN LYS PRO ALA ILE PHE MET ASP CYS GLY PHE
SEQRES 6 B 306 HIS ALA ARG GLU TRP ILE SER HIS ALA PHE CYS GLN TRP
SEQRES 7 B 306 PHE VAL ARG GLU ALA VAL LEU THR TYR GLY TYR GLU SER
SEQRES 8 B 306 HIS MET THR GLU PHE LEU ASN LYS LEU ASP PHE TYR VAL
SEQRES 9 B 306 LEU PRO VAL LEU ASN ILE ASP GLY TYR ILE TYR THR TRP
SEQRES 10 B 306 THR LYS ASN ARG MET TRP ARG LYS THR ARG SER THR ASN
SEQRES 11 B 306 ALA GLY THR THR CYS ILE GLY THR ASP PRO ASN ARG ASN
SEQRES 12 B 306 PHE ASP ALA GLY TRP CYS THR THR GLY ALA SER THR ASP
SEQRES 13 B 306 PRO CYS ASP GLU THR TYR CYS GLY SER ALA ALA GLU SER
SEQRES 14 B 306 GLU LYS GLU THR LYS ALA LEU ALA ASP PHE ILE ARG ASN
SEQRES 15 B 306 ASN LEU SER SER ILE LYS ALA TYR LEU THR ILE HIS SER
SEQRES 16 B 306 TYR SER GLN MET ILE LEU TYR PRO TYR SER TYR ASP TYR
SEQRES 17 B 306 LYS LEU PRO GLU ASN ASN ALA GLU LEU ASN ASN LEU ALA
SEQRES 18 B 306 LYS ALA ALA VAL LYS GLU LEU ALA THR LEU TYR GLY THR
SEQRES 19 B 306 LYS TYR THR TYR GLY PRO GLY ALA THR THR ILE TYR PRO
SEQRES 20 B 306 ALA ALA GLY GLY SER ASP ASP TRP ALA TYR ASP GLN GLY
SEQRES 21 B 306 ILE LYS TYR SER PHE THR PHE GLU LEU ARG ASP LYS GLY
SEQRES 22 B 306 ARG TYR GLY PHE ILE LEU PRO GLU SER GLN ILE GLN ALA
SEQRES 23 B 306 THR CYS GLU GLU THR MET LEU ALA ILE LYS TYR VAL THR
SEQRES 24 B 306 ASN TYR VAL LEU GLY HIS LEU
SEQRES 1 C 306 THR THR GLY HIS SER TYR GLU LYS TYR ASN ASN TRP GLU
SEQRES 2 C 306 THR ILE GLU ALA TRP THR LYS GLN VAL THR SER GLU ASN
SEQRES 3 C 306 PRO ASP LEU ILE SER ARG THR ALA ILE GLY THR THR PHE
SEQRES 4 C 306 LEU GLY ASN ASN ILE TYR LEU LEU LYS VAL GLY LYS PRO
SEQRES 5 C 306 GLY PRO ASN LYS PRO ALA ILE PHE MET ASP CYS GLY PHE
SEQRES 6 C 306 HIS ALA ARG GLU TRP ILE SER HIS ALA PHE CYS GLN TRP
SEQRES 7 C 306 PHE VAL ARG GLU ALA VAL LEU THR TYR GLY TYR GLU SER
SEQRES 8 C 306 HIS MET THR GLU PHE LEU ASN LYS LEU ASP PHE TYR VAL
SEQRES 9 C 306 LEU PRO VAL LEU ASN ILE ASP GLY TYR ILE TYR THR TRP
SEQRES 10 C 306 THR LYS ASN ARG MET TRP ARG LYS THR ARG SER THR ASN
SEQRES 11 C 306 ALA GLY THR THR CYS ILE GLY THR ASP PRO ASN ARG ASN
SEQRES 12 C 306 PHE ASP ALA GLY TRP CYS THR THR GLY ALA SER THR ASP
SEQRES 13 C 306 PRO CYS ASP GLU THR TYR CYS GLY SER ALA ALA GLU SER
SEQRES 14 C 306 GLU LYS GLU THR LYS ALA LEU ALA ASP PHE ILE ARG ASN
SEQRES 15 C 306 ASN LEU SER SER ILE LYS ALA TYR LEU THR ILE HIS SER
SEQRES 16 C 306 TYR SER GLN MET ILE LEU TYR PRO TYR SER TYR ASP TYR
SEQRES 17 C 306 LYS LEU PRO GLU ASN ASN ALA GLU LEU ASN ASN LEU ALA
SEQRES 18 C 306 LYS ALA ALA VAL LYS GLU LEU ALA THR LEU TYR GLY THR
SEQRES 19 C 306 LYS TYR THR TYR GLY PRO GLY ALA THR THR ILE TYR PRO
SEQRES 20 C 306 ALA ALA GLY GLY SER ASP ASP TRP ALA TYR ASP GLN GLY
SEQRES 21 C 306 ILE LYS TYR SER PHE THR PHE GLU LEU ARG ASP LYS GLY
SEQRES 22 C 306 ARG TYR GLY PHE ILE LEU PRO GLU SER GLN ILE GLN ALA
SEQRES 23 C 306 THR CYS GLU GLU THR MET LEU ALA ILE LYS TYR VAL THR
SEQRES 24 C 306 ASN TYR VAL LEU GLY HIS LEU
HET ZN A 400 1
HET 33Z A 401 44
HET ZN B 500 1
HET 33Z B 501 44
HET ZN C 600 1
HET 33Z C 601 44
HETNAM ZN ZINC ION
HETNAM 33Z (2S)-2-(3-{[AMINO(IMINO)METHYL]AMINO}PHENYL)-3-[(R)-
HETNAM 2 33Z [(1R)-1-({N-[(BENZYLOXY)CARBONYL]-L-
HETNAM 3 33Z PHENYLALANYL}AMINO)-2-METHYLPROPYL](HYDROXY)
HETNAM 4 33Z PHOSPHORYL]PROPANOIC ACID
FORMUL 4 ZN 3(ZN 2+)
FORMUL 5 33Z 3(C31 H38 N5 O7 P)
FORMUL 10 HOH *624(H2 O)
HELIX 1 1 ASN A 14 ASN A 29 1 16
HELIX 2 2 GLU A 72 TYR A 90 1 19
HELIX 3 3 GLU A 93 LEU A 103 1 11
HELIX 4 4 ASN A 112 LYS A 122 1 11
HELIX 5 5 ASP A 142 ASN A 146 5 5
HELIX 6 6 GLU A 173 ASN A 186 1 14
HELIX 7 7 ASN A 215 THR A 232 1 18
HELIX 8 8 GLY A 243 ILE A 247 1 5
HELIX 9 9 GLY A 253 GLN A 261 1 9
HELIX 10 10 PRO A 282 SER A 284 5 3
HELIX 11 11 GLN A 285 GLY A 306 1 22
HELIX 12 12 ASN B 14 ASN B 29 1 16
HELIX 13 13 GLU B 72 TYR B 90 1 19
HELIX 14 14 GLU B 93 LEU B 103 1 11
HELIX 15 15 ASN B 112 LYS B 122 1 11
HELIX 16 16 ASP B 142 ASN B 146 5 5
HELIX 17 17 GLU B 173 ASN B 186 1 14
HELIX 18 18 ASN B 215 GLY B 235 1 21
HELIX 19 19 GLY B 243 ILE B 247 1 5
HELIX 20 20 GLY B 253 GLN B 261 1 9
HELIX 21 21 PRO B 282 SER B 284 5 3
HELIX 22 22 GLN B 285 GLY B 306 1 22
HELIX 23 23 ASN C 14 ASN C 29 1 16
HELIX 24 24 GLU C 72 TYR C 90 1 19
HELIX 25 25 GLU C 93 LEU C 103 1 11
HELIX 26 26 ASN C 112 LYS C 122 1 11
HELIX 27 27 ASP C 142 ASN C 146 5 5
HELIX 28 28 GLU C 173 ASN C 186 1 14
HELIX 29 29 ASN C 215 THR C 232 1 18
HELIX 30 30 GLY C 243 ILE C 247 1 5
HELIX 31 31 GLY C 253 GLN C 261 1 9
HELIX 32 32 PRO C 282 SER C 284 5 3
HELIX 33 33 GLN C 285 GLY C 306 1 22
SHEET 1 A 8 ILE A 33 THR A 40 0
SHEET 2 A 8 ASN A 46 VAL A 52 -1 O LYS A 51 N SER A 34
SHEET 3 A 8 ASP A 104 LEU A 108 -1 O PHE A 105 N VAL A 52
SHEET 4 A 8 ALA A 61 CYS A 66 1 N MET A 64 O TYR A 106
SHEET 5 A 8 ILE A 189 HIS A 196 1 O LYS A 190 N ALA A 61
SHEET 6 A 8 TYR A 265 GLU A 270 1 O TYR A 265 N TYR A 192
SHEET 7 A 8 MET A 201 TYR A 204 -1 N LEU A 203 O THR A 268
SHEET 8 A 8 THR A 239 PRO A 242 1 O THR A 239 N ILE A 202
SHEET 1 B 8 ILE B 33 THR B 40 0
SHEET 2 B 8 ASN B 46 VAL B 52 -1 O LYS B 51 N SER B 34
SHEET 3 B 8 ASP B 104 LEU B 108 -1 O PHE B 105 N VAL B 52
SHEET 4 B 8 ALA B 61 CYS B 66 1 N MET B 64 O TYR B 106
SHEET 5 B 8 ILE B 189 HIS B 196 1 O LYS B 190 N ALA B 61
SHEET 6 B 8 TYR B 265 GLU B 270 1 O TYR B 265 N TYR B 192
SHEET 7 B 8 MET B 201 TYR B 204 -1 N LEU B 203 O THR B 268
SHEET 8 B 8 THR B 239 PRO B 242 1 O THR B 239 N ILE B 202
SHEET 1 C 8 ILE C 33 THR C 40 0
SHEET 2 C 8 ASN C 46 VAL C 52 -1 O LEU C 49 N THR C 36
SHEET 3 C 8 ASP C 104 LEU C 108 -1 O PHE C 105 N VAL C 52
SHEET 4 C 8 ALA C 61 ASP C 65 1 N MET C 64 O TYR C 106
SHEET 5 C 8 ILE C 189 HIS C 196 1 O LEU C 193 N PHE C 63
SHEET 6 C 8 TYR C 265 GLU C 270 1 O TYR C 265 N TYR C 192
SHEET 7 C 8 MET C 201 TYR C 204 -1 N LEU C 203 O THR C 268
SHEET 8 C 8 THR C 239 PRO C 242 1 O THR C 239 N ILE C 202
SSBOND 1 CYS A 66 CYS A 79 1555 1555 2.04
SSBOND 2 CYS A 138 CYS A 161 1555 1555 2.03
SSBOND 3 CYS A 152 CYS A 166 1555 1555 2.03
SSBOND 4 CYS B 66 CYS B 79 1555 1555 2.03
SSBOND 5 CYS B 138 CYS B 161 1555 1555 2.03
SSBOND 6 CYS B 152 CYS B 166 1555 1555 2.03
SSBOND 7 CYS C 66 CYS C 79 1555 1555 2.03
SSBOND 8 CYS C 138 CYS C 161 1555 1555 2.03
SSBOND 9 CYS C 152 CYS C 166 1555 1555 2.04
CISPEP 1 SER A 197 TYR A 198 0 -5.60
CISPEP 2 PRO A 205 TYR A 206 0 2.36
CISPEP 3 ARG A 272 ASP A 273 0 -7.36
CISPEP 4 SER B 197 TYR B 198 0 -1.98
CISPEP 5 PRO B 205 TYR B 206 0 0.90
CISPEP 6 ARG B 272 ASP B 273 0 -8.73
CISPEP 7 SER C 197 TYR C 198 0 -3.11
CISPEP 8 PRO C 205 TYR C 206 0 -1.70
CISPEP 9 ARG C 272 ASP C 273 0 -4.19
SITE 1 AC1 4 HIS A 69 GLU A 72 HIS A 196 33Z A 401
SITE 1 AC2 4 HIS B 69 GLU B 72 HIS B 196 33Z B 501
SITE 1 AC3 4 HIS C 69 GLU C 72 HIS C 196 33Z C 601
SITE 1 AC4 25 HIS A 69 ARG A 71 GLU A 72 ARG A 127
SITE 2 AC4 25 ASN A 144 ARG A 145 HIS A 196 SER A 197
SITE 3 AC4 25 TYR A 198 SER A 199 LEU A 203 SER A 207
SITE 4 AC4 25 ILE A 247 TYR A 248 ALA A 250 GLY A 253
SITE 5 AC4 25 ASP A 255 ASP A 256 GLU A 270 PHE A 279
SITE 6 AC4 25 ZN A 400 HOH A 443 HOH A 447 HOH A 465
SITE 7 AC4 25 HOH A 557
SITE 1 AC5 26 HIS B 69 ARG B 71 GLU B 72 ARG B 127
SITE 2 AC5 26 ASN B 144 ARG B 145 HIS B 196 SER B 197
SITE 3 AC5 26 TYR B 198 SER B 199 LEU B 203 SER B 207
SITE 4 AC5 26 ILE B 247 TYR B 248 ALA B 250 GLY B 253
SITE 5 AC5 26 ASP B 255 ASP B 256 GLU B 270 PHE B 279
SITE 6 AC5 26 ZN B 500 HOH B 538 HOH B 556 HOH B 564
SITE 7 AC5 26 HOH B 685 HOH B 709
SITE 1 AC6 23 HIS C 69 ARG C 71 GLU C 72 ARG C 127
SITE 2 AC6 23 ASN C 144 ARG C 145 GLU C 163 HIS C 196
SITE 3 AC6 23 SER C 197 TYR C 198 SER C 199 SER C 207
SITE 4 AC6 23 TYR C 248 GLY C 253 ASP C 255 ASP C 256
SITE 5 AC6 23 GLU C 270 PHE C 279 ZN C 600 HOH C 608
SITE 6 AC6 23 HOH C 639 HOH C 641 HOH C 696
CRYST1 66.964 96.379 135.641 90.00 90.00 90.00 P 21 21 21 12
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.014933 0.000000 0.000000 0.00000
SCALE2 0.000000 0.010376 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007372 0.00000
(ATOM LINES ARE NOT SHOWN.)
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